Evidence map›Paper›PMID 34109028›Full record

ArticleChemical science2020

Systematic quantification of the dynamics of newly synthesized proteins unveiling their degradation pathways in human cells.

Ming Tong, Johanna M Smeekens, Haopeng Xiao, Ronghu Wu

Open access · diamondAbstract read
In one paragraph

Article in Chemical science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed, 1 pooled it
1.5field-weighted citation impact, top 18% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

14 citing papers in PubMed, 1 synthesis or guideline pooled it, 26 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Maximum entropy determination of mammalian proteome dynamics.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. The TRiCky Business of Protein Folding in Health and Disease.Frontiers in cell and developmental biology · 2022
    Review
  13. Article
  14. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 2 countries.

Ming TongSchool of Chemistry and Biochemistry and the Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology Atlanta Georgia 30332 USA ronghu.wu@chemistry.gatech.edu +1-404-894-7452 +1-404-385-1515.
Johanna M SmeekensSchool of Chemistry and Biochemistry and the Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology Atlanta Georgia 30332 USA ronghu.wu@chemistry.gatech.edu +1-404-894-7452 +1-404-385-1515.
Haopeng XiaoSchool of Chemistry and Biochemistry and the Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology Atlanta Georgia 30332 USA ronghu.wu@chemistry.gatech.edu +1-404-894-7452 +1-404-385-1515.
Ronghu WuSchool of Chemistry and Biochemistry and the Petit Institute for Bioengineering and Bioscience, Georgia Institute of Technology Atlanta Georgia 30332 USA ronghu.wu@chemistry.gatech.edu +1-404-894-7452 +1-404-385-1515.ORCID https://orcid.org/0000-0001-9493-9462
Georgia Institute of Technology · US

Funding

Effective MS-Based Methods for Unraveling Cell Surface Protein InteractionsR01GM118803 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI WU, RONGHU · 2017 to 2024
$2.4M
NIGMS NIH HHS R01 GM118803
6 · The paper itself

Abstract

Proteins are continuously synthesized during cell growth and proliferation. At the same time, excessive and misfolded proteins have to be degraded, otherwise they are a burden to cells. Protein degradation is essential to maintain proteostasis in cells, and dysfunction of protein degradation systems results in numerous diseases such as cancer and neurodegenerative diseases. Despite the importance of protein degradation, the degradation pathways of many proteins remain to be explored. Here, we comprehensively investigated the degradation of newly synthesized proteins in human cells by integrating metabolic labeling, click chemistry, and multiplexed proteomics, and systematic and quantitative analysis of newly synthesized proteins first revealed the degradation pathways of many proteins. Bioinformatic analysis demonstrates that proteins degraded through two major pathways have distinct properties and functions. Proteins degraded through the ubiquitin-proteasome pathway contain more disordered structures, whereas those through the autophagy-lysosome pathway have significantly higher hydrophobicity. Systematic and quantitative investigation of the dynamics of newly synthesized proteins provides unprecedented and valuable information about protein degradation, which leads to a better understanding of protein properties and cellular activities.

Identifiers

PMID34109028
PMCPMC8152571
OpenAlexW3010831631

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.